Uptake of amino acids by actidione-treated yeast cells |
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Authors: | A. Kotyk L. Říhová M. Ponec |
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Affiliation: | 1. Laboratory for Cell Membrane Transport, Institute of Microbiology, Czechoslovak Academy of Sciences, Prague 4
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Abstract: | The active uptake ofl-aspartic acid, glycine andl-lysine by actidione-treated cells ofSaccharomyces cerevisiae was found to be inhibited by anaerobic conditions in the absence of a source of energy, only facilitated diffusion persisting. Similarly, metabolic inhibitors (iodoacetamide, sodium fluoride and potassium sorbate) inhibited the uptake very substantially. 2,4-Dinitrophenol and sodium azide appeared to inhibit the movement of the transport carrier itself, while uranyl ions showed a complex interaction pattern, ranging from inhibition at concentrations of 10?6–10?4 m, to stimulation at concentrations of 3×10?4–10?3 m, to pronounced inhibition at higher concentrations. The uptake was pH-dependent with optima forl-aspartic acid near pH 4, for glycine near pH 5, forl-lysine near pH 6.5. |
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